SEARCH · Search PubMed

Results for “CYTOPLASM”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 325 records · Page 18Linked to original sources

PubMed1997

Fluorogenic compound hydrolysis as a measure of toxicity-induced cytoplasmic viscosity and pH changes.

If a fluorogenic compound, such as fluorescein diacetate, is added to a water solution containing living cells it becomes hydrolyzed by intracellular esterases into a fluorochrome whose fluorescence can be used to monitor the cytoplasmic pH and the cytoplasmic viscosity of the cells. In this paper we have used this technique to measure the effects of different concentrations of Co2+ and Cd2+ ions on the cytoplasmic pH and the cytoplasmic viscosity of a single cell culture. Our results indicate that the observed decrease in the efficiency of the intracellular hydrolyzation of fluorogenic substances in the presence of different concentrations of heavy metals could be caused by both a decrease in the cytoplasmic pH and an increase in the cytoplasmic viscosity. A decrease in cytoplasmic pH would decrease the effectiveness of the intracellular enzymes, whereas an increase in cytoplasmic viscosity would decrease diffusion which would also reduce the effectiveness of the reaction. The dependence of the reciprocal of the cytoplasmic viscosity on the concentration of these metals correlates well with published results on their toxicity.

Journal Article↗

PubMed2003

In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli.

Gram-negative bacteria are able to convert potential energy inherent in the proton gradient of the cytoplasmic membrane into active nutrient transport across the outer membrane. The transduction of energy is mediated by TonB protein. Previous studies suggest a model in which TonB makes sequential and cyclic contact with proteins in each membrane, a process called shuttling. A key feature of shuttling is that the amino-terminal signal anchor must quit its association with the cytoplasmic membrane, and TonB becomes associated solely with the outer membrane. However, the initial studies did not exclude the possibility that TonB was artifactually pulled from the cytoplasmic membrane by the fractionation process. To resolve this ambiguity, we devised a method to test whether the extreme TonB amino-terminus, located in the cytoplasm, ever became accessible to the cys-specific, cytoplasmic membrane-impermeant molecule, Oregon Green(R) 488 maleimide (OGM) in vivo. A full-length TonB and a truncated TonB were modified to carry a sole cysteine at position 3. Both full-length TonB and truncated TonB (consisting of the amino-terminal two-thirds) achieved identical conformations in the cytoplasmic membrane, as determined by their abilities to cross-link to the cytoplasmic membrane protein ExbB and their abilities to respond conformationally to the presence or absence of proton motive force. Full-length TonB could be amino-terminally labelled in vivo, suggesting that it was periplasmically exposed. In contrast, truncated TonB, which did not associate with the outer membrane, was not specifically labelled in vivo. The truncated TonB also acted as a control for leakage of OGM across the cytoplasmic membrane. Further, the extent of labelling for full-length TonB correlated roughly with the proportion of TonB found at the outer membrane. These findings suggest that TonB does indeed disengage from the cytoplasmic membrane during energy transduction and shuttle to the outer membrane.

Bacterial Proteins↗

PubMedDate not supplied

Nuclear and cytoplasmic c-myc staining in endometrial carcinoma and their relationship to survival.

OBJECTIVE: The role of the c-myc proto-oncogene in genomic instability is just becoming more fully understood. However, its role in endometrial cancer is essentially unknown. The objective of this study was to determine the relationship between cytoplasmic and nuclear c-myc staining, DNA index, and survival in patients with endometrial carcinoma. METHODS: One hundred and twenty-one patients with endometrial carcinoma were studied. Image analysis was used to determine DNA index. In addition to cytoplasmic and nuclear c-myc staining and DNA index, histologic type, stage, grade, depth of invasion, lymphvascular space invasion, and peritoneal cytology were evaluated as prognostic indicators. Univariate and multivariate analyses were performed. RESULTS: One hundred and twenty-one patients were followed for over 5 years. c-myc cytoplasmic staining was present in 75.2% of the patients' tumors, and nuclear staining was present in 66.9% (P = 0.99). DNA index was significantly higher in patients with nuclear c-myc staining and no cytoplasmic staining (DNA index 1.38) as compared to those patients whose tumors displayed cytoplasmic c-myc staining but no nuclear c-myc staining (1.18) (P = 0.016). Patients whose tumors stained positively for nuclear c-myc and negatively for cytoplasmic c-myc had significantly worse survival by Kaplan-Meier analysis (P < 0.0001). Seventeen patients died during the follow-up period of this study. By multivariate analysis, positive cytoplasmic c-myc staining with negative nuclear staining (P = 0.0076), negative cytoplasmic c-myc staining with positive nuclear staining (P = 0.011) and FIGO stage (P < 0.0001) were shown to be independent prognostic indicators predictive of survival. CONCLUSION: Nuclear and cytoplasmic c-myc staining, as well as FIGO stage, when assessed by multivariate analysis, were demonstrated to be important factors in predicting survival in the 121 patients in this study. While increasing FIGO stage was prognostic of decreased survival, the specific location of c-myc staining was also associated with prognosis. The expression of the c-myc protein is related to survival in patients with adenocarcinoma of the endometrium.

Adenocarcinoma, Clear Cell↗

PubMed2002

Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5.

The efficient release of many enveloped viruses from cells involves the coalescence of viral components at sites of budding on the plasma membrane of infected cells. This coalescence is believed to require interactions between the cytoplasmic tails of surface glycoproteins and the matrix (M) protein. For the paramyxovirus simian virus 5 (SV5), the cytoplasmic tail of the hemagglutinin-neuraminidase (HN) protein has been shown previously to be important for normal virus budding. To investigate a role for the cytoplasmic tail of the fusion (F) protein in virus assembly and budding, we generated a series of F cytoplasmic tail-truncated recombinant viruses. Analysis of these viruses in tissue culture indicated that the cytoplasmic tail of the F protein was dispensable for normal virus replication and budding. To investigate further the requirements for assembly and budding of SV5, we generated two double-mutant recombinant viruses that lack 8 amino acids of the predicted 17-amino-acid HN protein cytoplasmic tail in combination with truncation of either 10 or 18 amino acids from the predicted 20-amino-acid F protein cytoplasmic tail. Both of the double mutant recombinant viruses displayed a replication defect in tissue culture and a budding defect, the extent of which was dependent on the length of the remaining F cytoplasmic tail. Taken together, this work and our earlier data on virus-like particle formation (A. P. Schmitt, G. P. Leser, D. L. Waning, and R. A. Lamb, J. Virol. 76:3953-3964, 2002) suggest a redundant role for the cytoplasmic tails of the HN and F proteins in virus assembly and budding.

Amino Acid Sequence↗

PubMed2004

Functional dissection of hnRNP D suggests that nuclear import is required before hnRNP D can modulate mRNA turnover in the cytoplasm.

Many shuttling proteins not only function in the nucleus but also control mRNA fates in the cytoplasm. We test whether a link exists between their nuclear association with mRNPs and their cytoplasmic functions using the p37 isoform of hnRNP D, which inhibits the rapid cytoplasmic mRNA decay in NIH3T3 cells. We showed that p37 shuttles between nucleus and cytoplasm, and narrowed down the nuclear import signal to a 50-amino-acid C-terminal domain. A p37 mutant missing this domain, still capable of associating with target mRNAs in vitro, was confined to the cytoplasm, where it was unable to block cytoplasmic mRNA turnover. Introducing heterologous shuttling domains to this mutant, thereby restoring its ability to enter the nucleus, concomitantly restored its cytoplasmic function. Association of p37 with its target mRNAs can only be detected when it can enter the nucleus. Our results suggest that nuclear import of hnRNP D is a prerequisite for it to exert its cytoplasmic function. This study provides a useful model system to elucidate the mechanisms by which "nuclear history" affects cytoplasmic mRNA fates.

Active Transport, Cell Nucleus↗

PubMed1998

Palmitoylation of the cytoplasmic domain of the neural cell adhesion molecule N-CAM serves as an anchor to cellular membranes.

The neural cell adhesion molecule N-CAM is expressed at key sites during embryonic development and mediates homophilic adhesion between cells both in the embryo and in the adult. N-CAM is expressed in multiple forms and two of the major isoforms differ in their cytoplasmic domains, one (ld form) having an insert of 261 amino acids that is missing in the other (sd form). N-CAM has been previously shown to be palmitoylated, but the sites of acylation have not been localized. We show here that the cytoplasmic domain of the N-CAM became palmitoylated after transfection of a cDNA encoding N-CAM into COS-7 cells, and that this acylation occurs on the four closely spaced cysteines in the cytoplasmic domain of N-CAM. Moreover, when a cDNA encoding only the cytoplasmic domain was transfected into cells, the protein was palmitoylated and associated with membranes even though it lacked a membrane spanning segment. Site directed mutagenesis of the four cysteine residues to serines at positions 5, 11, 16, and 22 in the cytoplasmic domain (723, 729, 734, and 740 in the native protein) eliminated both the palmitoylation and association with the membrane fraction. Mutagenesis of the cysteines individually, in pairs, and in groups of three indicated that C5 is not acylated with either palmitate or oleate, but the other three cysteines are acylated to different extents. Cytoplasmic domains with single cysteine mutations localized primarily in the membrane fraction, while those with three mutations were found primarily in the cytoplasm. Proteins containing two mutated cysteines were found in both the cytoplasm and the membrane fraction with C11 and C16 having the most influence on the distribution in accord with their higher level of acylation. Mutation of the cysteines did not affect the ability of full-length N-CAM to promote aggregation when transfected into COS-7 cells. Based on these results we suggest that the primary role of palmitoylation is to provide a second anchor in the plasma membrane to direct the protein to discrete membrane microdomains or to organize the cytoplasmic region for interaction with factors that affect signaling events resulting from N-CAM mediated adhesion.

Acylation↗

PubMed1993

Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine.

To investigate the contribution of the cytoplasmic domain of the vesicular stomatitis virus G glycoprotein to its basolateral expression in polarized epithelial cells, chimeric proteins containing the external and transmembrane domains of an apically targeted protein, the influenza virus hemagglutinin (HA), and either the G cytoplasmic domain or an unrelated cytoplasmic sequence, were introduced into Madin-Darby canine kidney (MDCK) cells. Addition of the cytoplasmic tail of G to a truncated HA resulted in delivery of greater than 95% of the chimeric protein to the basolateral cell surface, indicating that the G cytoplasmic domain contains a dominant basolateral sorting signal. A similar chimera, containing the cytoplasmic tail of herpes simplex I glycoprotein gC, was not sorted basolaterally. Deletion of the cytoplasmic tail from G protein itself decreased the fidelity of sorting to the basolateral surface, but not the extent to which the protein reached the plasma membrane. Mutation of cytoplasmic tyrosine 501 of G caused an identical loss of basolateral targeting, suggesting that the tyrosine, or the sequence surrounding it, is required for efficient basolateral transport of G. Mutation of tyrosine 501 had no effect on internalization of G, which was much slower than that of endocytic receptors. Thus, VSV G protein contains an efficient cytoplasmic basolateral targeting signal that is not an efficient internalization signal.

Amino Acid Sequence↗

PubMed1999

What is new with anti-neutrophil cytoplasmic antibodies: diagnostic, pathogenetic and therapeutic implications.

Anti-neutrophil cytoplasmic antibodies, as detected by indirect immunofluorescence, have limited diagnostic significance as they occur in a variety of inflammatory disorders. The presence of antibodies to defined target antigens of anti-neutrophil cytoplasmic antibodies, that is proteinase 3 and myeloperoxidase, is, however, highly specific for one of the systemic vasculitides, in particular Wegener's granulomatosis, microscopic polyangiitis, Churg-Strauss syndrome, and idiopathic pauci-immune necrotizing crescentic glomerulonephritis. In general, anti-proteinase-3-positive patients show more widespread organ involvement, more granuloma formation, and a more severe initial course of their renal lesions than anti-myeloperoxidase-positive patients; however, there is considerable overlap, and either antibody specificity may be found in the different clinical syndromes. In vitro, anti-neutrophil cytoplasmic antibodies are able further to activate pre-activated neutrophils and monocytes, which can result in endothelial damage. A direct activating effect of anti-neutrophil cytoplasmic antibodies on endothelial cells has been suggested, but those studies should be confirmed. In vivo, experimental data support a pathogenetic role for anti-neutrophil cytoplasmic antibodies, particularly anti-myeloperoxidase, but besides anti-neutrophil cytoplasmic antibodies a second pro-inflammatory stimulus seems to be required to induce lesions. Whether anti-neutrophil cytoplasmic antibodies can be a direct target for treatment has still to be proved. Current immunosuppressive treatment regimens for the anti-neutrophil cytoplasmic antibody-associated vasculitides are, however, unsatisfactory because of side-effects, that is opportunistic infections and malignancies. New treatment regimens, based on new pathogenetic concepts, are currently being tested.

Animals↗

PubMed1965

ELECTRON MICROSCOPE OBSERVATIONS ON INTACT CELLS, PROTOPLASTS, AND THE CYTOPLASMIC MEMBRANE OF BACILLUS STEAROTHERMOPHILUS.

Abram, Dinah (Purdue University, Lafayette, Ind.). Electron microscope observations on intact cells, protoplasts, and the cytoplasmic membrane of Bacillus stearothermophilus. J. Bacteriol. 89:855-873. 1965.-Negatively stained preparations of protoplasts and fragments of cytoplasmic membranes from cells of Bacillus stearothermophilus ruptured by treatment with sonic oscillation, partial lysis with lysozyme, autolysis, or phage infection were examined electron microscopically. Specimens of intact cells also were examined by the same technique. The following structural details were revealed. Intact or nearly intact, partially swollen, elongated protoplasts and their ghosts have a characteristic differentiated surface texture and can easily be distinguished from the cell wall. Infoldings of the cytoplasmic membrane can be observed in these protoplasts, to which flagella are attached; the latter originate via hooks from "basal structures" that are in close association with the cytoplasmic membrane or part of it. Abundant intracytoplasmic membranous elements, which appear to be tubular or vesicular, can be seen in whole cells of three of the strains studied. The fine structure of the cytoplasmic membrane and probably that of its intracytoplasmic infoldings was observed on flattened and folded membrane fragments, one layer thick. Structural units, roughly spherical, 65 to 85 A in diameter, were present on one side of the cytoplasmic membrane, facing the cytoplasm. They were attached loosely to the membrane by fine stalks, 40 to 60 A long, and were easily detached, probably leaving the stalks behind them on the membrane. While the greater stability of membranes from thermophiles made this study of the fine structure possible, the structural units described were demonstrated also on cytoplasmic membranes from mesophiles.

Bacillus↗

PubMed2006

Mechanisms for human cytomegalovirus-induced cytoplasmic p53 sequestration in endothelial cells.

Human cytomegalovirus (HCMV) infection results in endothelial dysfunction, typically known as dysregulated apoptosis, and aberrant expression and sub-cellular localization of p53, a tumor suppressor that accumulates at the late stage of infection. In this study, we examined three hypotheses that could be responsible for HCMV-induced cytoplasmic p53 accumulation at the later stage of infection: hyperactive nuclear export, cytoplasmic p53 tethering and delayed p53 degradation. Leptomycin B treatment, a nuclear export inhibitor, was unable to reduce cytoplasmic p53, thereby eliminating the hyperactive nuclear export mechanism. The findings that nascent p53 still entered nuclei after the nuclear export inhibition indicated that cytoplasmic tethering may play a minor role. Cytoplasmic p53 was still observed after the translation activities were blocked by cycloheximide. There was more than an eight-fold increase in the cytoplasmic p53 half-life with abnormal p53 ubiquitination. Taken together, these results suggest that delayed degradation could be responsible for the cytoplasmic p53 accumulation. The general slow-down of the proteasomal activity and the dysregulated p53 ubiquitination process at the later stage of infection could contribute to the reduced cytoplasmic p53 degradation and might be relevant to dysregulated endothelial apoptosis. The HCMV-induced changes in p53 dynamics could contribute to endothelial dysfunction.

Apoptosis↗

PubMed1987

Comparative study of cytoplasmic elimination in spermatids of selected mammalian species.

In the transformation of a spermatid into a spermatozoon, cytoplasmic loss occurs, allowing the sperm to swim unhindered. Cytoplasmic loss takes place via elimination of the residual body and through structures known as tubulobulbar complexes. A determination of cytoplasmic loss in several species was undertaken by using high-resolution electron microscopic morphometric techniques. During the period that tubulobulbar complexes are present, an average 53% cytoplasmic loss was recorded for five species (guinea pig, 48.8 +/- 6.2% (SEM); monkey, 60.3 +/- 4.3%; opossum, 54.5 +/- 4.4%; rabbit, 46.9 +/- 2.7%; and rat, 55.7 +/- 4.9%), whereas there was essentially no loss or gain in cytoplasm during the same period for round spermatids. Surprisingly, during spermatid elongation an approximate 36% loss of cytoplasm was also recorded for five species (guinea pig, 50.1 +/- 6.3%; monkey, 30.0 +/- 15.4%; opossum, 25.4 +/- 9.0%; rabbit, 42.4 +/- 8.6%; and rat, 34.9 +/- 11.9%), which is only partially (approximately 60%) accounted for by fluid pumping from the nucleus during nuclear condensation. A densification of the cytoplasm of elongate spermatids, as compared with round spermatids, suggests fluid is also pumped from the elongating spermatid cytoplasm. Fluid loss from germ cells may contribute to the seminiferous tubule fluid, a fluid previously thought to be solely of Sertoli-cell origin.

Animals↗

PubMed2004

Dissociation of double-headed cytoplasmic dynein into single-headed species and its motile properties.

Cytoplasmic dynein is a minus-end directed microtubule motor and plays important roles in the transport of various intracellular cargoes. Cytoplasmic dynein comprises two identical heavy chains and forms a dimer (double-headed dynein); the total molecular weight of the cytoplasmic dynein complex is about 1.5 million. The dynein motor domain is structurally very different from those of kinesin and myosin, and our understanding of the mechanisms of dynein energy transduction is limited mainly because of the difficulty in obtaining a sufficient quantity of purified and active cytoplasmic dynein. We purified cytoplasmic dynein, which was free from dynactin and other dynein-associated proteins. The purified cytoplasmic dynein was active in an in vitro motility assay. The controlled dialysis of the purified dynein against 4 M urea resulted in its complete dissociation into monomeric species (single-headed dynein). The separation of the dynein heads by the treatment was reversible. The MgATPase activities of the single-headed and reconstituted double-headed dynein were comparable to that of intact dynein. The double-headed dynein bundled microtubules in the absence of ATP; the single-headed dynein did not. The single-headed dynein produced in vitro microtubule-gliding motility at velocities very similar to those of double-headed dynein at various ATP concentrations. These results indicate that a single cytoplasmic dynein heavy chain is sufficient to produce robust microtubule motility. Application of the double- and single-headed dynein molecules in various assay systems will elucidate the mechanism of action of the cytoplasmic dynein.

Animals↗

PubMed2001

p53 Mutations are present in colorectal cancer with cytoplasmic p53 accumulation.

Previous studies have shown that nuclear p53 over-expression is an indicator of p53 mutations whereas cytoplasmic p53 accumulation is related to wild-type p53 in several kinds of tumors. Cytoplasmic p53 accumulation has been demonstrated to be an independent prognostic factor in colorectal adenocarcinomas. The purpose was to examine whether mutations occur in cases with p53 accumulated in the cytoplasm and whether there are any differences in the frequency and characteristics of p53 mutations in different staining patterns. In the present study, we identified p53 mutations using PCR single-strand conformation polymorphism (SSCP) and DNA sequencing in 75 primary colorectal adenocarcinomas with different staining patterns (negative, nucleus, cytoplasm, nucleus and cytoplasm). The results show that the frequency and nature of mutations in tumors with cytoplasmic p53 accumulation were similar to those with nuclear p53 expression. However, the tumors with accumulation in both the nucleus and cytoplasm demonstrated a higher mutation rate. We suppose that the role of cytoplasmic p53 accumulation in predicting prognosis in patients with colorectal cancer may be dependent on both mutational and non-mutational mechanisms.

Biomarkers, Tumor↗

PubMedDate not supplied

Large changes in cytoplasmic biopolymer concentration with osmolality indicate that macromolecular crowding may regulate protein-DNA interactions and growth rate in osmotically stressed Escherichia coli K-12.

From determination of amounts and concentrations of biopolymers and solutes in the cytoplasm of Escherichia coli, we are obtaining information needed to assess the effect of macromolecular crowding on cytoplasmic properties and processes of osmotically stressed bacteria. We observe that growth rate, and the amount of cytoplasmic water decrease and cytoplasmic concentrations of biopolymers and K+, increase with increasing osmolality, even for cells grown in the presence of osmoprotectants like glycine betaine. We observe general correlations between the amount of cytoplasmic water, growth rate and cytoplasmic K+ concentration in osmotically stressed cells grown both with and without osmoprotectants. To explain these correlations, we propose that crowding increases with increasing growth osmolality, which in turn buffers the binding of proteins to nucleic acids against changes in cytoplasmic K+ concentration and (by affecting biopolymer diffusion rates and/or assembly equilibria) is a determinant of growth rate of osmotically stressed cells. Changes in biopolymer concentration and crowding may also explain the increase of the activity coefficient of cytoplasmic water with increasing osmolality of growth in E. coli.

Betaine↗

PubMed1990

Desmin and actin associated with cytoplasmic bodies in skeletal muscle fibers: immunocytochemical and fine structural studies, with a note on unusual 18- to 20-nm filaments.

In a fine structural and immunocytochemical study, the latter performed on semithin sections of epoxy resin embedded skeletal muscle fibers, three types of cytoplasmic bodies were identified in a case of cytoplasmic body myopathy: (1) The first type, the classical type, showed a central core and a light halo with radiating actin filaments at the periphery. (2) The second type, the spheroid body was characterized by irregularly arranged granular masses associated with intermediate filaments. Desmin immunoreactivity occurred in the central and peripheral parts, where filaments of intermediate size were visualized by electron microscopy. Desmin immunoreactivity was noted also at the Z-bands of striated annulets, within areas of disordered myofibrils, such as sarcoplasmic masses, and in atrophic muscle fibers. (3) The third type of the cytoplasmic body was composed mainly of large masses of uneven granularity and electron density. The center of this type reacted to anti-actin antibody suggesting that the 5- to 6-nm filaments, which ultrastructurally proved to be a major component, were of the actin type. By contrast, neither intermediate filaments nor actin microfilaments were found by electron microscopy in cytoplasmic bodies in a second case where no immunoreaction to desmin or actin occurred. Anti-vimentin antibody stained only the cytoplasm of endomysial cells, but not the inclusion bodies. Some other, unusual inclusions with 18- to 20-nm tubulo-filamentous structures have to be distinguished from the various types of filaments in cytoplasmic bodies. It is concluded, that pleomorphism and heterogeneity of "cytoplasmic bodies" have to be taken into consideration when classifying cytoplasmic body myopathies.

Actins↗

PubMed2000

Antineutrophil cytoplasmic antibodies in inflammatory bowel disease: clinical role and review of the literature.

PURPOSE: Perinuclear antineutrophil cytoplasmic antibodies have been found consistently in patients with ulcerative colitis; however, their pathogenetic and clinical role is still uncertain. In this study we tested the prevalence of perinuclear antineutrophil cytoplasmic antibodies in a large population of patients with ulcerative colitis and Crohn's disease, with particular attention to the possible correlation with clinical features. METHODS: Perinuclear antineutrophil cytoplasmic antibody reactivity was investigated with indirect immunofluorescence in 279 patients with ulcerative colitis, 110 patients with Crohn's disease, and 252 unrelated healthy subjects. RESULTS: Perinuclear antineutrophil cytoplasmic antibodies were found in 84 of 279 patients with ulcerative colitis (30 percent), 10 of 110 patients with Crohn's disease (9 percent), and 2 of 252 healthy subjects (<1 percent; P < 0.001), respectively. Perinuclear antineutrophil cytoplasmic antibodies were significantly more frequent in patients with ulcerative colitis with higher relapse rate (43 vs. 27 percent; P < 0.002), and patients with Crohn's disease with colitis (27 vs. 2.5 percent; P < 0.0003). Perinuclear antineutrophil cytoplasmic antibodies were also significantly less frequent in patients with ulcerative colitis in remission (18 vs. 34 percent; P < 0.0025). CONCLUSIONS: In this study we confirm the relative specificity of perinuclear antineutrophil cytoplasmic antibodies, either for ulcerative colitis or for Crohn's disease involving the colon. Perinuclear antineutrophil cytoplasmic antibodies were more frequently found in patients with ulcerative colitis with a more aggressive clinical behavior; however, their presence had a limited value in identifying homogeneous subgroups of patients in our population.

Adolescent↗

PubMed1990

The cytoplasmic HBVDNA implication: HBV replication or non-replicative status.

Intrahepatocellular HBVDNA was investigated in patients with chronic hepatitis B by in situ hybridization assay, employing biotin-labelled HBVDNA as the specific probe. It was found that HBVDNA was predominantly present in the cytoplasm of hepatocytes. In general the cases with cytoplasmic HBVDNA could be grouped as follows: 1) cytoplasmic HBVDNA coinciding with intrahepatic envelope protein and nucleocapsid component expression, this pattern of the cytoplasmic HBVDNA would be replicative; 2) cytoplasmic HBVDNA accompanied by intrahepatic single HBsAg expression, common to HBVDNA integrated into host genome with only HBsAg being found frequently in liver; 3) with only cytoplasmic HBVDNA, with neither HBsAg nor HBcAg expression, representative for non-replicative status. It is speculated that the reason for the occurrence of the cytoplasmic hybridization signal in cases with non-replicative HBVDNA may be due to DNA-RNA transcript hybrid. The prudent way to evaluate the implication of the cytoplasmic HBVDNA is to consider the combination of HBVDNA location, intrahepatic gene product expression, and HBV markers in the serum.

Cytoplasm↗

PubMed1996

Differences in hydration state of nucleus and cytoplasm of the amphibian oocyte.

Nuclear magnetic resonance (NMR) microimaging and proton relaxation times were used to monitor differences between the hydration state of the nucleus and cytoplasm in the Rana pipiens oocyte. Individual isolated ovarian oocytes were imaged in a drop of Ringer's solution with an in-plane resolution of 80 microm. Proton spin echo images of oocytes arrested in prophase I indicated a marked difference in contrast between nucleoplasm and cytoplasm with additional intensity gradations between the yolk platelet-rich region of the cytoplasm and regions with little yolk. Neither shortening taue (spin echo time) to 9 msec (from 18 msec) nor lengthening taur (spin recovery time) to 2 sec (from 0.5 sec) reduced the observed contrast between nucleus and cytoplasm. Water proton T1 (spin-lattice) relaxation times of oocyte suspensions indicated three water compartments that corresponded to extracellular medium (T1 = 3.0 sec), cytoplasm (T1 = 0.8 sec) and nucleoplasm (T1 = 1.6 sec). The 1.6 sec compartment disappeared at the time of nuclear breakdown. Measurements of plasma and nuclear membrane potentials with KCl-filled glass microelectrodes demonstrated that the prophase I oocyte nucleus was about 25 mV inside positive relative to the extracellular medium. A model for the prophase-arrested oocyte is proposed in which a high concentration of large impermeant ions together with small counter ions set up a Donnan-type equilibrium that results in an increased distribution of water within the nucleus in comparison with the cytosol. This study indicates: (i) a slow exchange between two or more intracellular water compartments on the NMR time-scale, (ii) an increased rotational correlation time for water molecules in both the cytoplasmic and nuclear compartments compared to bulk water, and (iii) a higher water content (per unit dry mass) of the nucleus compared to the cytoplasm, and (iv) the existence of a large (about 75 mV positive) electropotential difference between the nuclear and cytoplasmic compartments.

Animals↗